ABSTRACT
Abstract The aim of this study was to analyze the structural, morphological and mechanical properties of two different lithium disilicate glass-reinforced ceramics for CAD-CAM systems (IPS e.max CAD and Rosetta SM). Five methodologies were used for both ceramics: microstructure (n = 2) was analyzed using x-ray diffraction (XRD); morphological properties (n = 2) were analyzed by scanning electron microscopy (SEM), with and without hydrofluoric etching; porosity (n = 3) was assessed using 3D micro-computed tomography (micro-CT); flexural strength was measured (n =1 0) using the three-point bending test; and bond strength was determined with self-adhesive resin cement (n = 10), using a microshear bond test. After performing all the tests, the data were analyzed using t-Student test and two-way ANOVA. All the tests used a significance level of α = 0.05. High peak positions corresponding to standard lithium metasilicate and lithium disilicate with similar intensities were observed for both ceramics in the XRD analysis. Morphological analysis showed that the crystalline structure of the two ceramics studied showed no statistical difference after acid etching. Additionally, no significant differences were recorded in the number or size of the pores for the ceramics evaluated. Moreover, no differences in flexural strength were found for the ceramic materials tested, or in the bond strength to ceramic substrates for the resin cements. Based on the study results, no significant differences were found between the two CAD-CAM lithium disilicate glass-reinforced ceramics tested, since they presented similar crystalline structures with comparable intensities, and similar total porosity, flexural strength and bond strength.
Subject(s)
Ceramics/chemistry , Computer-Aided Design , Dental Porcelain/chemistry , Glass/chemistry , Reference Values , Surface Properties , X-Ray Diffraction , Materials Testing , Microscopy, Electron, Scanning , Reproducibility of Results , Analysis of Variance , Porosity , Dental Bonding/methods , Resin Cements/chemistry , Shear Strength , Flexural StrengthABSTRACT
Background: Snake venoms are a complex mixture of proteins, organic and inorganic compounds. Some of these proteins, enzymatic or non-enzymatic ones, are able to interact with platelet receptors, causing hemostatic disorders. The possible therapeutic potential of toxins with antiplatelet properties may arouse interest in the pharmacological areas. The present study aimed to purify and characterize an antiplatelet DC protein from Bothrops alternatus snake venom. Methods: The protein, called BaltDC (DC protein from B. alternatus snake venom), was purified by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. The molecular mass was estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). The amino acid sequence of the N-terminal region was carried out by Edman degradation method. Platelet aggregation assays were performed in human platelet-rich plasma (PRP). Infrared (IR) spectroscopy was used in order to elucidate the interactions between BaltDC and platelet membrane. Results: BaltDC ran as a single protein band on SDS-PAGE and showed apparent molecular mass of 32 kDa under reducing or non-reducing conditions. The N-terminal region of the purified protein revealed the amino acid sequence IISPPVCGNELLEVGEECDCGTPENCQNECCDA, which showed identity with other snake venom metalloproteinases (SVMPs). BaltDC was devoid of proteolytic, hemorrhagic, defibrinating or coagulant activities, but it showed a specific inhibitory effect on platelet aggregation induced by ristocetin and epinephrine in PRP. IR analysis spectra strongly suggests that PO 3 2 − groups, present in BaltDC, form hydrogen bonds with the PO 2 − groups present in the non-lipid portion of the membrane platelets. Conclusions: BaltDC may be of medical interest since it was able to inhibit platelet aggregation.(AU)
Subject(s)
Animals , Snake Venoms , Spectrum Analysis , Platelet Aggregation , Bothrops , Hemostatic Disorders , Metalloproteases , Sodium Dodecyl Sulfate , Electrophoresis, Polyacrylamide GelABSTRACT
Abstract Background: Snake venoms are a complex mixture of proteins, organic and inorganic compounds. Some of these proteins, enzymatic or non-enzymatic ones, are able to interact with platelet receptors, causing hemostatic disorders. The possible therapeutic potential of toxins with antiplatelet properties may arouse interest in the pharmacological areas. The present study aimed to purify and characterize an antiplatelet DC protein from Bothrops alternatus snake venom. Methods: The protein, called BaltDC (DC protein from B. alternatus snake venom), was purified by a combination of ion-exchange chromatography on DEAE-Sephacel column and gel filtration on Sephadex G-75. The molecular mass was estimated by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate (SDS-PAGE). The amino acid sequence of the N-terminal region was carried out by Edman degradation method. Platelet aggregation assays were performed in human platelet-rich plasma (PRP). Infrared (IR) spectroscopy was used in order to elucidate the interactions between BaltDC and platelet membrane. Results: BaltDC ran as a single protein band on SDS-PAGE and showed apparent molecular mass of 32 kDa under reducing or non-reducing conditions. The N-terminal region of the purified protein revealed the amino acid sequence IISPPVCGNELLEVGEECDCGTPENCQNECCDA, which showed identity with other snake venom metalloproteinases (SVMPs). BaltDC was devoid of proteolytic, hemorrhagic, defibrinating or coagulant activities, but it showed a specific inhibitory effect on platelet aggregation induced by ristocetin and epinephrine in PRP. IR analysis spectra strongly suggests that PO 3 2 groups, present in BaltDC, form hydrogen bonds with the PO 2 groups present in the non-lipid portion of the membrane platelets. Conclusions: BaltDC may be of medical interest since it was able to inhibit platelet aggregation.